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Key Documents

SAB3500884

Sigma-Aldrich

Monoclonal Anti-HIV-1 P24-Biotin antibody produced in mouse

clone 8G9, affinity isolated antibody

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

conjugate

biotin conjugate

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

8G9, monoclonal

form

buffered aqueous solution

species reactivity

virus

concentration

1 mg/mL

technique(s)

ELISA: suitable
immunoblotting: suitable

NCBI accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Immunogen

Antibody was raised against a recombinant full-length HIV-1 p24 protein.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Supplied at 1 mg/mL in PBS with 0.02% sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Barbara J Flynn et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(17), 7131-7136 (2011-04-07)
Protein vaccines, if rendered immunogenic, would facilitate vaccine development against HIV and other pathogens. We compared in nonhuman primates (NHPs) immune responses to HIV Gag p24 within 3G9 antibody to DEC205 ("DEC-HIV Gag p24"), an uptake receptor on dendritic cells
T Goto et al.
Micron (Oxford, England : 1993), 29(2-3), 123-138 (1998-07-31)
The life-cycle of human immunodeficiency virus type 1 (HIV-1) has been studied using several techniques including immunoelectron microscopy and cryomicroscopy. The HIV-1 particle consists of an envelope, a core and the region between the core and the envelope (matrix). Virus
E O Freed
Virology, 251(1), 1-15 (1998-11-14)
The Gag proteins of HIV-1, like those of other retroviruses, are necessary and sufficient for the assembly of virus-like particles. The roles played by HIV-1 Gag proteins during the life cycle are numerous and complex, involving not only assembly but

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